6JHY

Crystal Structure of the S1 subunit N-terminal domain from DcCoV UAE-HKU23 spike protein

Summary for 6JHY

• Entry DOI: 10.2210/pdb6jhy/pdb
• Descriptor: Spike protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: dccov uae-hku23; spike (s); n-terminal domain (ntd); crystal structure, viral protein
• Biological source: Dromedary camel coronavirus HKU23
• Total number of polymer chains: 1
• Total formula weight: 33913.23

Authors

Lu, G.,Cheng, Y.,Ye, F. (deposition date: 2019-02-19, release date: 2019-07-24, Last modification date: 2024-10-30)

Primary citation

Cheng, Y.,He, B.,Yang, J.,Ye, F.,Lin, S.,Yang, F.,Chen, Z.,Chen, Z.,Cao, Y.,Lu, G.
Crystal structure of the S1 subunit N-terminal domain from DcCoV UAE-HKU23 spike protein.
Virology, 535:74-82, 2019

PubMed Abstract: The DcCoV UAE-HKU23 coronavirus is a newly-found betacoronavirus (betaCoV) that can infect human cells. The viral spike protein plays pivotal roles in mediating receptor-recognition and membrane-fusion, and is therefore a key factor involved in viral pathogenesis and inter-species transmission. Here we reported the structural and functional characterization of the spike N-terminal domain (NTD) from DcCoV UAE-HKU23 (HKU23-NTD). Via mucin-binding assays, we showed that HKU23-NTD is able to bind sugars. We further solved the structure of HKU23-NTD, performed structure-guided mutagenesis and successfully located the potential sugar-binding pockets in the structure. Furthermore, via comparison of available betaCoV NTD structures, we demonstrated that betaCoV NTDs contain a conserved β-sandwich core, but exhibit variant folds in the peripheral elements located in the top-ceiling region and on the lateral side. While showing different compositions and structures, these peripheral elements are topologically equivalent β-sandwich-core insertions, highlighting a divergent evolution process for betaCoVs to form different lineages.

PubMed: 31279241
DOI: 10.1016/j.virol.2019.06.015

Experimental method

X-RAY DIFFRACTION (2.5 Å)